In Search of Functional Advantages of Knots in Proteins.

Détails

Ressource 1Télécharger: journal.pone.0165986.PDF (4035.92 [Ko])
Etat: Public
Version: Final published version
ID Serval
serval:BIB_B15CF13C8D83
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
In Search of Functional Advantages of Knots in Proteins.
Périodique
PLoS One
Auteur(s)
Dabrowski-Tumanski P., Stasiak A., Sulkowska J.I.
ISSN
1932-6203 (Electronic)
ISSN-L
1932-6203
Statut éditorial
Publié
Date de publication
2016
Peer-reviewed
Oui
Volume
11
Numéro
11
Pages
e0165986
Langue
anglais
Résumé
We analysed the structure of deeply knotted proteins representing three unrelated families of knotted proteins. We looked at the correlation between positions of knotted cores in these proteins and such local structural characteristics as the number of intra-chain contacts, structural stability and solvent accessibility. We observed that the knotted cores and especially their borders showed strong enrichment in the number of contacts. These regions showed also increased thermal stability, whereas their solvent accessibility was decreased. Interestingly, the active sites within these knotted proteins preferentially located in the regions with increased number of contacts that also have increased thermal stability and decreased solvent accessibility. Our results suggest that knotting of polypeptide chains provides a favourable environment for the active sites observed in knotted proteins. Some knotted proteins have homologues without a knot. Interestingly, these unknotted homologues form local entanglements that retain structural characteristics of the knotted cores.

Pubmed
Web of science
Open Access
Oui
Création de la notice
28/11/2016 12:56
Dernière modification de la notice
20/08/2019 15:20
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